Results 241 to 250 of about 159,783 (279)
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A novel reaction of reticulocyte peptide-chain elongation factor, EF2, with guanosine nucleotides
Archives of Biochemistry and Biophysics, 1973Abstract The formation of phenylalanyl puromycin from phenylalanyl-tRNA, bound nonenzymically or enzymically to reticulocyte ribosomes, requires the peptide-chain elongation factor, EF2 2 , and GTP. However the GTP analogue, GDPCP, may replace GTP to a significant extent in this reaction.
T, Lee, P, Tsai, R, Heintz
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European Journal of Biochemistry, 1985
The binding of [3H]cholesteryl 14‐methylhexadecanoate by a highly purified peptide elongation factor 1 from rabbit reticulocytes is significantly enhanced by GTP and CTP, much less by guanosine 5′‐[β,γ‐methylene]‐triphosphate and not at all by ATP or UTP.
Z, Tuhácková, J, Hradec
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The binding of [3H]cholesteryl 14‐methylhexadecanoate by a highly purified peptide elongation factor 1 from rabbit reticulocytes is significantly enhanced by GTP and CTP, much less by guanosine 5′‐[β,γ‐methylene]‐triphosphate and not at all by ATP or UTP.
Z, Tuhácková, J, Hradec
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Nature, 1969
At least two molecules of GTP may be hydrolysed during the addition of an amino-acid to a growing peptide chain.
Peter Lengyel
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At least two molecules of GTP may be hydrolysed during the addition of an amino-acid to a growing peptide chain.
Peter Lengyel
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The Journal of Biochemistry, 1989
The cytoplasmic peptide elongation factor, EF-1 alpha, is anchored at the endoplasmic reticulum membrane by phosphatidylinositol via ethanolamine bridging presumably to Asp306 of the protein.
Y, Hayashi, R, Urade, S, Utsumi, M, Kito
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The cytoplasmic peptide elongation factor, EF-1 alpha, is anchored at the endoplasmic reticulum membrane by phosphatidylinositol via ethanolamine bridging presumably to Asp306 of the protein.
Y, Hayashi, R, Urade, S, Utsumi, M, Kito
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IUBMB Life, 1996
AbstractThis investigation has shown it is possible to purify elongation factor‐2 from livers of two rather distinct animal species, minks and chicken, to high homogeneity by employing the same purification procedure. It is also shown that making peptide maps of the factor by the use of Staphylococcus aureus Endoprotease Glu‐C gives the same pattern ...
Bent Riis
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AbstractThis investigation has shown it is possible to purify elongation factor‐2 from livers of two rather distinct animal species, minks and chicken, to high homogeneity by employing the same purification procedure. It is also shown that making peptide maps of the factor by the use of Staphylococcus aureus Endoprotease Glu‐C gives the same pattern ...
Bent Riis
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Journal of Molecular Biology, 2008
The elongation stage of protein synthesis consists of repeated cycles of the binding of aminoacyl-tRNA, peptide bond formation, and translocation. The process is normally catalyzed by the elongation factors Tu and G; however, the reactions can proceed, at least in prescribed and limited circumstance, in the absence of the elongation factors, a finding ...
Yuen-Ling Chan, Ira G Wool
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The elongation stage of protein synthesis consists of repeated cycles of the binding of aminoacyl-tRNA, peptide bond formation, and translocation. The process is normally catalyzed by the elongation factors Tu and G; however, the reactions can proceed, at least in prescribed and limited circumstance, in the absence of the elongation factors, a finding ...
Yuen-Ling Chan, Ira G Wool
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Nature, 1968
The amino-acid polymerization factors S1 and S3 form complexes with most aminoacyl-tRNA species, including met-tRNAM, but not F-met-tRNAF and not met-tRNAF. This discrimination may be a basis for avoiding one kind of ambiguity in translation.
Y, Ono +3 more
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The amino-acid polymerization factors S1 and S3 form complexes with most aminoacyl-tRNA species, including met-tRNAM, but not F-met-tRNAF and not met-tRNAF. This discrimination may be a basis for avoiding one kind of ambiguity in translation.
Y, Ono +3 more
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European Journal of Biochemistry, 1990
EF‐Tu is often referred to as a model for guanine‐nucleotide‐binding regulatory proteins (G‐proteins), since X‐ray diffraction analysis of its GTP‐binding domain shows a detailed location of the ‘consensus’ amino acid sequences involved in nucleotide binding.
B, Kraal +5 more
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EF‐Tu is often referred to as a model for guanine‐nucleotide‐binding regulatory proteins (G‐proteins), since X‐ray diffraction analysis of its GTP‐binding domain shows a detailed location of the ‘consensus’ amino acid sequences involved in nucleotide binding.
B, Kraal +5 more
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Biochemical and Biophysical Research Communications, 1975
The primary structure around the sulfhydryl groups of the polypeptide chain elongation factor Tu has been investigated. The tryptic peptides containing sulfhydryl groups were separated from other peptides by affinity chromatography using a p-chloromercuribenzoate-agarose column.
S, Nakamura +3 more
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The primary structure around the sulfhydryl groups of the polypeptide chain elongation factor Tu has been investigated. The tryptic peptides containing sulfhydryl groups were separated from other peptides by affinity chromatography using a p-chloromercuribenzoate-agarose column.
S, Nakamura +3 more
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Functional Role and Biochemical Properties of Yeast Peptide Elongation Factor 3 (EF-3)
1990The eukaryotic peptide elongation cycle is well known to be driven by the two complementary factors EF-lα and EF-2, functionally analogous to the bacterial EF-Tu and EF-G, respectively, and the two GTP hydrolysis steps catalyzed by those factors have been considered to be essential for the cycle to run (Kaziro, 1978; Moldave, 19 85). On yeast ribosomes,
Masazumi Miyazaki +4 more
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